Regulation of cloned cardiac channels

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dc.contributorDavis, Michael
dc.contributorLessard, Charles
dc.creatorBalasubramanian, Bharathi
dc.date.accessioned2005-11-01T15:44:46Z
dc.date.accessioned2017-04-07T19:50:24Z
dc.date.available2005-11-01T15:44:46Z
dc.date.available2017-04-07T19:50:24Z
dc.date.created2005-08
dc.date.issued2005-11-01
dc.description.abstractActivation of a5??1 integrin potentiates L-type calcium current in vascular smooth muscle, which is partly mediated by tyrosine phoshorylation of the a1c channel subunit. Expressed rabbit VSM and neuronal isoforms are also potentiated by a5??1 integrin activation and require dual phosphorylation of a1c by PKA and c-Src. To explore common mechanisms of regulation by a5??1 integrin, whole cell patch clamp experiments were used to investigate the effects of a5??1 integrin antibody on expressed cardiac calcium channels. In HEK cells transfected with a1c, ??2a and a2-d1 subunits alone, currents increased 1.8 ?? 2.0 fold on application of a5??1 antibody. The potentiation was almost completely abolished on the application of PKI, a highly specific Protein Kinase A (PKA) inhibitor. The expressed currents increased 2.0 ?? 2.2 fold on application of PKA activator 8-Br-cAMP, and abolished by PKI. Our results suggest that regulation of L-type calcium channels by a5??1 integrin is a general mechanism shared by VSM, neuronal and cardiac channels. However, in the cardiac isoform, only PKA phosphorylation is involved.
dc.identifier.urihttp://hdl.handle.net/1969.1/2525
dc.language.isoen_US
dc.publisherTexas A&M University
dc.subjectpatch clamp
dc.subjectcalcium channels
dc.titleRegulation of cloned cardiac channels
dc.typeBook
dc.typeThesis

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